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Figure 2
Characterization of bromophenoxy propanamide (1) binding to oxidized BpsDsbA by 2D [15N,1H]-HSQC NMR. (a) Expanded regions of the 2D [15N,1H]-HSQC data highlighting the backbone amide chemical shift perturbation (CSP) for selected residues of BpsDsbA without (blue) and with (red) 2 mM fragment 1. (b) CSP observed for each BpsDsbA residue. (c) CSPs resulting from the addition of 2 mM fragment 1 are mapped onto the crystal structure of oxidized BpsDsbA (PDB entry 4k2d) as a colour gradient from red (CSP = 0.04 p.p.m.) to white (CSP = 0 p.p.m.). Non-shifting residues are shown in grey. Residues with unassigned amides and proline residues are shown in black. N-terminal residues (Ala1–Gly14) were removed for clarity.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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